Studies will be continued on the conformation change that is postulated for coenzyme A transferase in the enzyme-CoA intermediate. The postulated slow proton removal from fumarase will be examined using buffers and traps for the protonated enzyme. Rates of reaction of calcium ATPase with acyl phosphates will be examined under different conditions in an attempt to elucidate the mechanism of the phosphorylation step and the role of the nucleotide moiety of ATP. Equilibrium constants for the steps of this enzyme will be investigated. Solvent trapping experiments using water-trifluoroethanol and protonation and deuteration from water and deuterium oxide will be used to investigate the lifetime of carbonium ion and carbanion intermediates.